Abstract
When diethyl pyrocarbonate was used during the isolation of tRNA from bovine muscle, a preparation was obtained which was free of ribonuclease activity. This preparation, however, showed a loss of acceptor activity for several amino acids when compared to a preparation isolated without diethyl pyrocarbonate. Although there was no loss of acceptor activity for either histidine or tyrosine, there were significant changes in the reversed-phase freon chromatographic profile for these amino acids. Similar chromatographic changes could be produced by reacting a nuclease-free preparation of bovine lens tRNA with diethyl pyrocarbonate for 5 min at 37°, thereby suggesting a modification of the tRNA by diethyl pyrocarbonate.
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